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Murine V kappa 25 and V kappa 27 amino-acid sequences of C57B1/6 origin: monoclonal antibodies 17S29.1 and 22S25.1 specific for the group A-streptococcal polysaccharide.

  • Aebersold, R
  • Herbst, H
  • Grütter, T
  • Chang, J Y
  • Braun, D G
Published Article
Hoppe-Seyler's Zeitschrift für physiologische Chemie
Publication Date
Dec 01, 1984
PMID: 6441768


Antibodies 17S29.1 and 22S25.1 are monoclonal, hybridoma-derived gamma 3 kappa murine immunoglobulins with specificity for N-acetyl-glucosamine beta 1----3-linked to the L-rhamnose backbone structure, the immunodeterminant of the streptococcal Group A polysaccharide. The VL 17S29.1 amino-acid sequence is the third complete one reported from an antibody with this specificity, the second fully determined V kappa 25 structure and the first complete V kappa sequence of C57B1/6 origin derived from a carbohydrate-specific antibody. VL22S25.1 is a member of the V kappa 27 isotype of murine immunoglobulin VL regions. V kappa 17S29.1 and the determined part of the V kappa 22S25.1 sequence are compared to the previously described V kappa regions of streptococcal Group A polysaccharide-specific antibodies and to 12 selected partial and complete V kappa regions of antibodies with other specificities, predominantly to carbohydrate antigens. Both V kappa 17S29.1 and V kappa 22S25.1 increase the variability of known murine V kappa regions. They are the most homologous to the other V kappa regions derived from antibodies with streptococcal Group A polysaccharide specificity and share with them the amino-acid residue Arg74, so far characteristic for V kappa regions from antibodies with this specificity. The analysis of groups of independently expressed, highly homologous V kappa regions, namely V kappa 17S29.1 and V kappa 2S1.3 as one and V kappa 7S34.1 and V kappa 22S25.1 as a second group, offers the possibility of estimating the minimal number of V kappa germline genes involved in the immune response to the structurally defined streptococcal Group A polysaccharide antigen.(ABSTRACT TRUNCATED AT 250 WORDS)


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